{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Morra G"],"funding":["NEI NIH HHS"],"pagination":["1208-1217.e2"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9356978"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["30(8)"],"pubmed_abstract":["Class A (rhodopsin-like) G protein-coupled receptors (GPCRs) are constitutive phospholipid scramblases as evinced after their reconstitution into liposomes. Yet phospholipid scrambling is not detectable in the resting plasma membrane of mammalian cells that is replete with GPCRs. We considered whether cholesterol, a prominent component of the plasma membrane, limits the ability of GPCRs to scramble lipids. Our previous Markov State Model (MSM) analysis of molecular dynamics simulations of membrane-embedded opsin indicated that phospholipid headgroups traverse a dynamically revealed hydrophilic groove between transmembrane helices (TM) 6 and 7 while their tails remain in the bilayer. Here, we present comparative MSM analyses of 150-μs simulations of opsin in cholesterol-free and cholesterol"],"journal":["Structure (London, England : 1993)"],"pubmed_title":["Cholesterol occupies the lipid translocation pathway to block phospholipid scrambling by a G protein-coupled receptor."],"pmcid":["PMC9356978"],"funding_grant_id":["P30 EY005722","R01 EY027969","R21 EY028314"],"pubmed_authors":["Morra G","Menon AK","Razavi AM","Khelashvili G"],"additional_accession":[]},"is_claimable":false,"name":"Cholesterol occupies the lipid translocation pathway to block phospholipid scrambling by a G protein-coupled receptor.","description":"Class A (rhodopsin-like) G protein-coupled receptors (GPCRs) are constitutive phospholipid scramblases as evinced after their reconstitution into liposomes. Yet phospholipid scrambling is not detectable in the resting plasma membrane of mammalian cells that is replete with GPCRs. We considered whether cholesterol, a prominent component of the plasma membrane, limits the ability of GPCRs to scramble lipids. Our previous Markov State Model (MSM) analysis of molecular dynamics simulations of membrane-embedded opsin indicated that phospholipid headgroups traverse a dynamically revealed hydrophilic groove between transmembrane helices (TM) 6 and 7 while their tails remain in the bilayer. Here, we present comparative MSM analyses of 150-μs simulations of opsin in cholesterol-free and cholesterol","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-06-02T08:22:27.618Z","creation":"2026-05-26T03:07:12.982Z"},"accession":"S-EPMC9356978","cross_references":{"pubmed":["35660161"],"doi":["10.1016/j.str.2022.05.010"]}}